Researchers fold a protein within a protein
Scientists have recently discovered a way to fold a protein within a protein. This is a very important find as some proteins were always hard to fold, and were exposed to elements that could denature them. Difficult to fold recombinant proteins are complex and often cost a lot when used in clinical and industrial applications. This new technology was developed using Archeoglobus fulgidus. This bacteria is found in hydrothermal vents and it has evolved unique solutions for protein folding and stabilization due to the conditions in which they live. Ferritin is an iron carrying 24- subunit protein found in the bacteria and its function is to store and carry iron in the blood. It is able to do so due to the tiny pores in the shell that provide small molecules access into the cavity. It also dissociates at low salt concentrations, so the contents of the cavity can be released when the pH is switched from 8.0 to 5.8. The exoshell also increased the yield of GFP, HRP and Renilla luciferase.
This exoshell technology is a breakthrough for science because it will make harder to fold proteins now more foldable. It also protects the proteins from denaturants that could destroy it. I believe this will help the world as we can now protect proteins at a lower cost. This will make research and possibly medication more available at a lower cost. This is good as many more scientists will be able to access these resources. I found and attached another article that explains protein folding and its function.